ID A8LPX0_DINSH Unreviewed; 1037 AA.
AC A8LPX0;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Valine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_02004};
DE EC=6.1.1.9 {ECO:0000256|HAMAP-Rule:MF_02004};
DE AltName: Full=Valyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_02004};
DE Short=ValRS {ECO:0000256|HAMAP-Rule:MF_02004};
GN Name=valS {ECO:0000256|HAMAP-Rule:MF_02004,
GN ECO:0000313|EMBL:ABV93824.1};
GN OrderedLocusNames=Dshi_2087 {ECO:0000313|EMBL:ABV93824.1};
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV93824.1, ECO:0000313|Proteomes:UP000006833};
RN [1] {ECO:0000313|Proteomes:UP000006833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC {ECO:0000313|Proteomes:UP000006833};
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC inadvertently accommodate and process structurally similar amino acids
CC such as threonine, to avoid such errors, it has a 'posttransfer'
CC editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC dependent manner. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC Evidence={ECO:0000256|ARBA:ARBA00001624, ECO:0000256|HAMAP-
CC Rule:MF_02004};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC activity. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC one for editing. The misactivated threonine is translocated from the
CC active site to the editing site. {ECO:0000256|HAMAP-Rule:MF_02004}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC ValS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_02004}.
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DR EMBL; CP000830; ABV93824.1; -; Genomic_DNA.
DR RefSeq; WP_012178757.1; NC_009952.1.
DR AlphaFoldDB; A8LPX0; -.
DR STRING; 398580.Dshi_2087; -.
DR KEGG; dsh:Dshi_2087; -.
DR eggNOG; COG0525; Bacteria.
DR HOGENOM; CLU_001493_0_2_5; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000006833; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07962; Anticodon_Ia_Val; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 1.10.287.380; Valyl-tRNA synthetase, C-terminal domain; 1.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
DR HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR033705; Anticodon_Ia_Val.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR010978; tRNA-bd_arm.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR InterPro; IPR019499; Val-tRNA_synth_tRNA-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR InterPro; IPR002303; Valyl-tRNA_ligase.
DR PANTHER; PTHR11946:SF93; VALINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11946; VALYL-TRNA SYNTHETASES; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF10458; Val_tRNA-synt_C; 1.
DR PRINTS; PR00986; TRNASYNTHVAL.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_02004};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Coiled coil {ECO:0000256|HAMAP-Rule:MF_02004};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_02004};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_02004};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_02004};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_02004}; Reference proteome {ECO:0000313|Proteomes:UP000006833}.
FT DOMAIN 16..519
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 598..714
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 765..908
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT DOMAIN 969..1033
FT /note="Valyl-tRNA synthetase tRNA-binding arm"
FT /evidence="ECO:0000259|Pfam:PF10458"
FT MOTIF 45..55
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT MOTIF 681..685
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
FT BINDING 684
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02004"
SQ SEQUENCE 1037 AA; 114342 MW; 7040F0AD24D70C70 CRC64;
MPMEKTFNAA EAEPRLYARW EAEGCFAAGA NASRDETFCV MIPPPNVTGS LHMGHAFNNT
LQDILIRWKR MQGYDTLWQP GTDHAGIATQ MVTEREMAAN GEPTRAEMGR AKFLARVWEQ
KVKSRGTIIG QLKRIGASCD WSREAFTMGG ADGDPEKGNG PNFHDAVIKV FVDMYDKGLI
YRGKRLVNWD PHFETAISDL EVENIETPGH MWHFKYPLAG GETYEYVEKD ADGTVTLRET
RDYISIATTR PETMLGDGAV AVHPSDERYA PIVGKLCEIP VGPKEHRRLI PIITDEYPDP
TFGSGAVKIT GAHDFNDYQV AKRGGIPMYR LMDTKARMRD DGAPYAKAAA IAMEVAEGTR
TLDEAEADSL NLVPDDLRGL DRFEARKAVV DQITAEGLAV MVPNPAAAAS TEEGAAATEE
VPAFLPLVES KPIMQPFGDR SKVVIEPMLT DQWFVDAEQI VGPALDAVRN GTVKILPESG
EKTYYHWLDN IEPWCISRQL WWGHQIPVWY GPRRVEVNGV ETLDFDPANA VHFVAHSVDE
ARAKAAGYYA LPDADKVIIV RSFPRGTPGS GPTDGRVDPM TDAVAAAQRA EAVPDAIPLV
QDPDVLDTWF SSGLWPIGTL GWPEDTEELR KYFPTSTLVT GQDILFFWVA RMMMMQLAVT
GEVPFREVYL HGLVRDAKGK KMSKSVGNVV DPLEIIDEYG ADALRFSSAA MASLGGVLKL
DLQRVQGYRN FGTKLWNATR FAEMNEVFTA HTQSAMPPGC TETVNRWIIG ETAKVREAVD
TALAEYKFND AANALYAFVW GKVCDWYVEF AKPLLLDGDD ATKAETRAVM AWVLDQCFIL
LHPIMPFITE ELWGTTGQRD KMLVHADWPS YGADLVDADA DREMNWVISL IESVRSVRAQ
MRVPAGLYVP VVQVALDEAG QRAYANNETL IKRLARIEGI TKADTAPKGA LTIPVEGGTF
ALPLADIIDV SAEKDRLGKT LAKLQKDLGG LRGRLSNAKF VASAPAEVVE ENRERLAAGE
AELATLSAAL ERLEEVG
//
